Opheline kinase
| Opheline kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.3.7 | ||||||||
| CAS no. | 37278-15-2 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Opheline kinase (EC 2.7.3.7) is an enzyme that catalyzes the reversible chemical reaction
The enzyme characterised from the marine annelid, Ophelia neglecta converts guanidinoethyl methyl phosphate (opheline) to the phosphagen, N'-phosphoguanidinoethyl methylphosphate, by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1] Unlike similar kinases such as lombricine kinase, the enzyme can phosphorylate a wider range of substrates including lombricine and taurocyamine.[2]
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:guanidinoethyl-methyl-phosphate phosphotransferase.[3]
References
- ↑ Thoai NV, di Jeso F, Robin Y, der Terrossian E (1966). "Sur la nouvelle acide adenosine 5'-triphosphorique:guanidine phosphotransferase, l'opheline kinase". Biochim. Biophys. Acta. 113: 542–550. doi:10.1016/s0926-6593(66)80012-7.
- ↑ Petkowski, Janusz J.; Bains, William; Seager, Sara (2019). "Natural Products Containing 'Rare' Organophosphorus Functional Groups". Molecules. 24 (5): 866. doi:10.3390/molecules24050866. PMC 6429109. PMID 30823503.
- ↑ Enzyme 2.7.3.7 at KEGG Pathway Database.